RT Journal Article
T1 A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron
A1 Hunter, Thérèse
A1 Bonetta, Rosalin
A1 Sacco, Anthony
A1 Vella, Marita
A1 Sultana, Paul-Michael
A1 Trinh, Chi H.
A1 Fadia, Hava B. R.
A1 Borowski, Tomasz
A1 García Fandiño, Rebeca
A1 Stockner, Thomas
A1 Hunter, Gary J.
K1 Enzymes
K1 Iron
K1 Manganese
K1 Metalloprotein
K1 Superoxide dismutase
AB We have generated a site‐directed mutant of the manganese superoxide dismutase SOD‐3 of C.elegans (MnSOD‐3) which modifies the metal specificity of the enzyme. While wild‐type MnSOD‐3 functions with manganese in the active site (3600 U mg−1 of protein) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50 % of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron
PB Wiley
YR 2018
FD 2018
LK http://hdl.handle.net/10347/24312
UL http://hdl.handle.net/10347/24312
LA eng
NO T. Hunter, R. Bonetta, A. Sacco, M. Vella, P.-M. Sultana, C. H. Trinh, H. B. R. Fadia, T. Borowski, R. Garcia-Fandiño, T. Stockner, G. J. Hunter, Chem. Eur. J. 2018, 24, 5303
NO Work reported here was carried out using funding from UoM grants PHBIN02‐1, PHBRP03‐05 and PHBRP03‐17. The European Union Erasmus+ programme (project number: 2016‐1‐PL01‐KA103‐023786) is acknowledged for providing financial support for the mobility traineeship of T.B. This research was supported in part by PL‐Grid Infrastructure. We wish to thank the EU COST association for support through COST actions CM1305 and CM1306
DS Minerva
RD 23 abr 2026